Render Target: STATIC
Render Timestamp: 2024-11-21T13:31:53.637Z
Commit: 5c4accf06eb7154018ba3f54329c7590f97f534a
XML generation date: 2024-10-16 18:03:08.432
Product last modified at: 2024-09-30T13:15:07.684Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Phospho-Tau (Ser199) Antibody #29957

Filter:
  • WB

    Supporting Data

    REACTIVITY H M R
    SENSITIVITY Endogenous
    MW (kDa) 50-80
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Phospho-Tau (Ser199) Antibodyrecognizes endogenous levels of Tau protein only when phosphorylated at Ser199. This antibody also detects a 110 kDa band of unknown origin.

    Species Reactivity:

    Human, Mouse, Rat

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser199 of human Tau protein. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    Tau is a heterogeneous microtubule-associated protein that promotes and stabilizes microtubule assembly, especially in axons. Six isoforms with different amino-terminal inserts and different numbers of tandem repeats near the carboxy terminus have been identified, and tau is hyperphosphorylated at approximately 25 sites by Erk, glycogen synthase kinase-3 (GSK-3), and CDK5 (1,2). Phosphorylation decreases the ability of tau to bind to microtubules. Neurofibrillary tangles are a major hallmark of Alzheimer's disease (AD); these tangles are bundles of paired helical filaments (PHFs) composed of hyperphosphorylated tau. In particular, phosphorylation at Ser396 by GSK-3 or CDK5 destabilizes microtubules. Furthermore, research studies have shown that inclusions of tau are found in a number of other neurodegenerative diseases, collectively known as tauopathies (1,3).

    Ser199 of Tau is phosphorylated by various kinases such as GSK-3β, AMP-activated protein kinase (AMPK), and dual specificity tyrosine-phosphorylation-regulated kinase 1A (Dyrk1A) (4-7). Phosphorylation of Ser199 of Tau is an early event in the pathogenesis of Alzheimer's disease (8,9).
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